MolNFT v1 · #175538 · protein

Open form of pet-degrading cutinase CUT190 with thermostability- improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation

7CTS · ALPHA/BETA hydrolase family protein: “Open form of pet-degrading cutinase CUT190 with thermostability- improving mutations of…”. X-ray diffraction, 2 ligands (BCN, CA), 1 pocket (best druggability 0.31). MolNFT v1 #175538 on…

PDB: 7CTS
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase family protein
EC: 3.1.1.74
UniProt: W0TJ64
Ligands: BCN, CA
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase family protein (EC 3.1.1.74)	protein	262	31% helix, 22% strand	W0TJ64

Ligands and binding sites

BCN · Bicine · ligand · chains A
CA · Calcium ion · metal · chains A
DIO · 1,4-diethylene dioxide · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.31	0.74	16	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7CTS · Open form of PET-degrading cutinase Cut190 with thermostability-improving mutations of… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt W0TJ64
Elsewhere: RCSB PDB 7CTS · PDBe 7CTS · UniProt W0TJ64

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